L-arabinose isomerase

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L-arabinose isomerase
4r1q.jpg
L-arabinose isomerase hexamer, Geobacillus kaustophilus
Identifiers
EC number5.3.1.4
CAS number9023-80-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Arabinose isomerase
PDB 2ajt EBI.jpg
crystal structure of l-arabinose isomerase from e.coli
Identifiers
SymbolArabinose_Isome
PfamPF02610
InterProIPR003762

In enzymology, a L-arabinose isomerase (EC 5.3.1.4) is an enzyme that catalyzes the chemical reaction

L-arabinose L-ribulose

Hence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose.

This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and glucuronate interconversions.

This enzyme catalyses the conversion of L-arabinose to L-ribulose as the first step in the pathway of L-arabinose utilization as a carbon source.[1]

Structural studies[edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2AJT and 2HXG.

References[edit]

  1. ^ Sa-Nogueira I, Nogueira TV, Soares S, de Lencastre H (March 1997). "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression". Microbiology. 143 (3): 957–69. doi:10.1099/00221287-143-3-957. PMID 9084180.

Further reading[edit]

  • HEATH EC, HORECKER BL, SMYRNIOTIS PZ, TAKAGI Y (1958). "Pentose fermentation by Lactobacillus plantarum. II. L-arabinose isomerase". J. Biol. Chem. 231 (2): 1031–7. PMID 13539034.
  • Nakamatu T, Yamanaka K (1969). "Crystallization and properties of L-arabinose isomerase from Lactobacillus gayonii". Biochim. Biophys. Acta. 178 (1): 156–65. doi:10.1016/0005-2744(69)90142-9. PMID 5773448.
This article incorporates text from the public domain Pfam and InterPro: IPR003762